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IB Biology > 8.1 Metabolism > Flashcards

8.1 Metabolism Flashcards

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1
Q

What is metabolism?

A

The sum total of all reactions that occur within an organism in order to maintain life

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2
Q

What causes most chemical changes in a cell?

A

A series of reactions

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3
Q

What controls each steps of series of reactions?

A

specific enzymes

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4
Q

Why do metabolic pathways allow for a greater level of regulation?

A

As the chemical change is controlled by numerous intermediates

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5
Q

What are metabolic pathways typically organised into?

A

Chains or cycles of enzyme catalysed reactions

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6
Q

What does every chemical reaction require in order to proceed?

A

A certain amount of energy

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7
Q

What is the energy needed in order to proceed called?

A

Activation energy

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8
Q

How do enzymes speed up the rate of a biochemical reaction?

A

By lowering the activation energy

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9
Q

What happens when an enzyme binds to a substrate?

A

It stresses and i the bonds in the substrate

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10
Q

What happens when the energy level of the substrates is reduced to the transitionary state?

A

Less energy is needed to convert into a product thus the reaction happens faster

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11
Q

What is an exergonic reaction?

A

If the reactants contain more energy than the products, the free energy is released into the system

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12
Q

What is an endergonic reaction?

A

If the reactants contain less energy than the products, free energy is lost to the system

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13
Q

What type of reactions are exergonic?

A

Catabolic

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14
Q

Why are exergonic reactions usually catabolic?

A

As energy is released from broken bonds within a molecule

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15
Q

What type of reactions are endergonic reactions?

A

Anabolic

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16
Q

Why are endergonic reactions normally anabolic?

A

As energy is required to synthesise bonds between molecules

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17
Q

What is an enzyme inhibitor?

A

A molecule that disrupts the normal reaction pathway between an enzyme and a substrate

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18
Q

What are the two types of enzyme inhibitors?

A

Competitive or non competitive

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19
Q

What do enzyme inhibitors prevent?

A

The formation of an enzyme substrate complex and thus any product

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20
Q

Why may the inhibition of enzymes be reversible or irreversible?

A

Depending on the specific effect of the inhibitor being used

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21
Q

What is an example of a competitive inhibitor?

A

Relenza

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22
Q

What is an example of a non competitive inhibitor?

A

Cyanide as poison

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23
Q

What do substrates do in a normal reaction?

A

Bind to an enzyme to form an enzyme substrate complex

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24
Q

What results in enzyme substrate specifity?

A

The fact that the shape and properties of active site and substrate are complementary

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25
Q

During a normal enzyme reaction what happens when binding occurs?

A

The active site undergoes a conformational change to optimally interact with the substrate

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26
Q

During a normal enzyme reaction, what does the conformational change do?

A

Destabilises chemical bonds in the substrate which lowers the activation energy

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27
Q

What is a consequence of enzyme interaction?

A

The substrate is converted into product at an accelerated rate

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28
Q

What is competitive inhibition?

A

Involves a molecule other than the substrate, binding to the enzymes active site

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29
Q

Why is the inhibitor molecule able to bind to the active site?

A

As it is structurally and chemically similar to the substrate

30
Q

What does the competitive inhibitor do?

A

Blocks the active site and stops substrate binding

31
Q

How can you reduce the effects of the inhibitor?

A

Increasing substrate concentration

32
Q

What is non competitive inhibition?

A

Involves a molecule binding to a site other than the active site

33
Q

What is the site that a non competitive inhibitor binds to?

A

An allosteric site

34
Q

What does the inhibitor binding to the allosteric site cause?

A

A conformational change to the enzymes active site

35
Q

In non competitive inhibition what does the change in the active site cause?

A

The active site and substrate aren’t complementary and thus the substrate cannot bind

36
Q

Why does increasing the substrate levels not mitigate non competitive inhibitors effects?

A

As the inhibitor is not in direct competition with the substrate

37
Q

What is end product inhibition?

A

A form of negative feedback by which metabolic pathways can be controlled

38
Q

What is the function of end product inhibition?

A

To ensure levels of an essential product are always tightly regulated

39
Q

In end product inhibition, what happens if product levels build up?

A

The product inhibits the reaction pathway and decreases the rate of further product formation

40
Q

In end product inhibition, what happens if product levels drop?

A

The reaction pathway will proceed uninterrupted and the rate of product formation will increase

41
Q

In end product inhibition, what does the final product do?

A

Inhibits an enzyme from an earlier step in the sequence

42
Q

In end production inhibition, what does the product bind to?

A

An allosteric site

43
Q

In end product inhibition, what does the product do?

A

Temporarily inactivates the enzyme

44
Q

In end product inhibition, what happens as the enzyme can no longer function?

A

The reaction sequence is halted and the rate of product formation is decreased

45
Q

What is isoleucine?

A

An essential amino acid

46
Q

Where do you have to get isoleucine from and why?

A

From food sources as it is not synthesised by the body

47
Q

In plants and bacteria where is isoleucine synthesised from?

A

Theronine

48
Q

How many steps is the isoleucine reaction pathway?

A

Five

49
Q

What happens in the first step of the isoleucine reaction pathway?

A

Threonine is converted into an intermediate compound by an enzyme

50
Q

During the five step reaction pathway what does isoleucine function as?

A

A non competitive inhibitor

51
Q

How is the production of isoleucine an example of end product inhibition?

A

An excess production of isoleucine inhibits further synthesis

52
Q

What does the end product inhibition feedback of isoleucine ensure?

A

That isoleucine production does not cannibalise available stocks of theronine

53
Q

How can the rate of an enzyme catalysed reaction be calculated and plotted according to?

A

The time taken for the reaction to proceed

54
Q

What are the two ways time taken can be measured according to?

A

Amount of product formed or amount of substrate consumed

55
Q

What is reaction rate the inverse of?

A

Time taken

56
Q

What is the formula for rate of reaction?

A

1/time taken

57
Q

What factors influence the rate of an enzyme catalysed reaction?

A

Temperature
pH
Substrate concentration

58
Q

How do both competitive and non competitive inhibitors reduce the rate of reaction?

A

By limiting the amount of uninhibited enzyme available for reaction

59
Q

Can the maximum rate of enzyme reaction still be achieved with a competitive inhibitor?

A

Yes but a higher substrate concentration is required

60
Q

Can the maximum rate of enzyme activity be achieved with non competitive inhibitors?

A

No it is reduced

61
Q

When comparing the graphs of the effect of inhibition, from top to bottom what is the order?

A

Uninhibited
Competitive inhibitor
Non competitive inhibitor

62
Q

What is malaria?

A

A disease caused by parasitic protozoans

63
Q

What does the life cycle of the parasite require?

A

Both a human and mosquito host

64
Q

How is malaria transmitted?

A

Via mosquito bites

65
Q

What is responsible for the maturation and development of the parasite in both human and mosquito host?

A

Specific enzymes

66
Q

What has scientists sequencing the genome of infectious species of plasmodium done?

A

Helped determine the parasites proteome

67
Q

What has learning about the parasites proteome done?

A

Helped identify enzymes involved in parasitic metabolism as potential targets for inhibition

68
Q

What are the enzymes identified in the proteome screened against and why?

A

A bioinformatic database of chemicals to identify potential enzyme inhibitors

69
Q

What may happened when a promising compound is identified? (malaria)

A

It may be chemically modified to improve its binding affinity and lower its toxicity

70
Q

What is another way anti malarial medications can be synthesised?

A

Rational drug design

71
Q

What does rational drug design involve?

A

Computer modelling techniques to invent a compound that functions as inhibitor

72
Q

In rational drug design, how is a complimentary compound synthesised?

A

Using complementary chemistry

IB Biology (57 decks)

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